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CAZyme Information: MGYG000003114_00770

You are here: Home > Sequence: MGYG000003114_00770

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Clostridium sp900547475
Lineage Bacteria; Firmicutes_A; Clostridia; Clostridiales; Clostridiaceae; Clostridium; Clostridium sp900547475
CAZyme ID MGYG000003114_00770
CAZy Family GH43
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
927 102365.41 4.1949
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003114 3467094 MAG United States North America
Gene Location Start: 54925;  End: 57708  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.99

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH43 41 417 2.2e-112 0.9967741935483871

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd18832 GH43_GsAbnA-like 2.83e-157 42 412 1 332
Glycosyl hydrolase family 43 protein such as Geobacillus stearothermophilus endo-alpha-1,5-L-arabinanase AbnA. This glycosyl hydrolase family 43 (GH43) subgroup includes mostly enzymes with alpha-L-arabinofuranosidase (ABF; EC 3.2.1.55) and endo-alpha-L-arabinanase (ABN; EC 3.2.1.99) activities. It includes Geobacillus stearothermophilus T-6 NCIMB 40222 AbnA, Bacillus subtilis subsp. subtilis str. 168 (Abn2;YxiA;J3A;BSU39330) (Arb43B), and Thermotoga petrophila RKU-1 (AbnA;TpABN;Tpet_0637). These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. The GH43 ABN enzymes hydrolyze alpha-1,5-L-arabinofuranoside linkages while the ABF enzymes cleave arabinose side chains so that the combined actions of these two enzymes reduce arabinan to L-arabinose and/or arabinooligosaccharides. Many of these enzymes are different from other arabinases; they are organized into two different domains with a divalent metal cluster close to the catalytic residues to guarantee the correct protonation state of the catalytic residues and consequently the enzyme activity. These arabinan-degrading enzymes are important in the food industry for efficient production of L-arabinose from agricultural waste; L-arabinose is often used as a bioactive sweetener. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.
COG3507 XynB2 6.06e-68 43 588 31 506
Beta-xylosidase [Carbohydrate transport and metabolism].
cd08998 GH43_Arb43a-like 1.65e-53 42 410 1 276
Glycosyl hydrolase family 43 protein such as Bacillus subtilis subsp. subtilis str. 168 endo-alpha-1,5-L-arabinanase Arb43A. This glycosyl hydrolase family 43 (GH43) subgroup belongs to the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. The GH43 ABN enzymes hydrolyze alpha-1,5-L-arabinofuranoside linkages while the ABF enzymes cleave arabinose side chains so that the combined actions of these two enzymes reduce arabinan to L-arabinose and/or arabinooligosaccharides. Many of these enzymes such as the Bacillus subtilis arabinanase Abn2, that hydrolyzes sugar beet arabinan (branched), linear alpha-1,5-L-arabinan and pectin, are different from other arabinases; they are organized into two different domains with a divalent metal cluster close to the catalytic residues to guarantee the correct protonation state of the catalytic residues and consequently the enzyme activity. These arabinan-degrading enzymes are important in the food industry for efficient production of L-arabinose from agricultural waste; L-arabinose is often used as a bioactive sweetener. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.
cd08988 GH43_ABN 1.27e-52 43 410 1 276
Glycosyl hydrolase family 43. This glycosyl hydrolase family 43 (GH43) subgroup includes mostly enzymes with alpha-L-arabinofuranosidase (ABF; EC 3.2.1.55) and endo-alpha-L-arabinanase (ABN; EC 3.2.1.99) activities. These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. The GH43 ABN enzymes hydrolyze alpha-1,5-L-arabinofuranoside linkages while the ABF enzymes cleave arabinose side chains so that the combined actions of these two enzymes reduce arabinan to L-arabinose and/or arabinooligosaccharides. These arabinan-degrading enzymes are important in the food industry for efficient production of L-arabinose from agricultural waste; L-arabinose is often used as a bioactive sweetener. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.
pfam16369 GH43_C 5.66e-34 421 528 1 106
C-terminal of Glycosyl hydrolases family 43. This is the C-terminal of Glycosyl hydrolases family 43. It is around 100 residues in length from various Bacteroides species. The function of this family is unknown.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
BCZ46633.1 0.0 1 850 1 859
AGF59399.1 0.0 5 853 2 863
AOZ93014.1 0.0 37 847 51 862
BBF43826.1 0.0 29 860 41 862
APC41808.1 5.48e-269 1 623 1 630

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5HO0_A 1.97e-219 38 846 49 843
Crystalstructure of AbnA (closed conformation), a GH43 extracellular arabinanase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],5HO2_A Crystal structure of AbnA (open conformation), a GH43 extracellular arabinanase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],5HOF_A Crystal structure of AbnA, a GH43 extracellular arabinanase from Geobacillus stearothermophilus, in complex with arabinopentaose [Geobacillus stearothermophilus],5HP6_A Structure of AbnA, a GH43 extracellular arabinanase from Geobacillus stearothermophilus (a new conformational state) [Geobacillus stearothermophilus]
5HO9_A 6.40e-215 38 616 49 636
Structureof truncated AbnA (domains 1-3), a GH43 arabinanase from Geobacilllus stearothermophilus, in complex with arabinooctaose [Geobacillus stearothermophilus],5HO9_B Structure of truncated AbnA (domains 1-3), a GH43 arabinanase from Geobacilllus stearothermophilus, in complex with arabinooctaose [Geobacillus stearothermophilus]
2X8F_A 1.04e-92 16 530 12 469
Nativestructure of Endo-1,5-alpha-L-arabinanases from Bacillus subtilis [Bacillus subtilis],2X8F_B Native structure of Endo-1,5-alpha-L-arabinanases from Bacillus subtilis [Bacillus subtilis]
4KC7_A 2.28e-92 42 532 33 473
CrystalStructure of Endo-1,5-alpha-L-arabinanase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],4KC7_B Crystal Structure of Endo-1,5-alpha-L-arabinanase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],4KC7_C Crystal Structure of Endo-1,5-alpha-L-arabinanase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],4KC8_A Crystal Structure of Endo-1,5-alpha-L-arabinanase from Thermotoga petrophila RKU-1 in complex with TRIS [Thermotoga petrophila RKU-1],4KC8_B Crystal Structure of Endo-1,5-alpha-L-arabinanase from Thermotoga petrophila RKU-1 in complex with TRIS [Thermotoga petrophila RKU-1],4KC8_C Crystal Structure of Endo-1,5-alpha-L-arabinanase from Thermotoga petrophila RKU-1 in complex with TRIS [Thermotoga petrophila RKU-1]
2X8S_A 3.95e-92 16 531 12 470
CrystalStructure of the Abn2 D171A mutant in complex with arabinotriose [Bacillus subtilis],2X8S_B Crystal Structure of the Abn2 D171A mutant in complex with arabinotriose [Bacillus subtilis]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P42293 5.55e-92 16 530 12 469
Extracellular endo-alpha-(1->5)-L-arabinanase 2 OS=Bacillus subtilis (strain 168) OX=224308 GN=abn2 PE=1 SV=2
A5IKD4 1.14e-91 42 532 30 470
Extracellular endo-alpha-(1->5)-L-arabinanase OS=Thermotoga petrophila (strain ATCC BAA-488 / DSM 13995 / JCM 10881 / RKU-1) OX=390874 GN=Tpet_0637 PE=1 SV=1
P94522 6.20e-15 1 355 1 276
Extracellular endo-alpha-(1->5)-L-arabinanase 1 OS=Bacillus subtilis (strain 168) OX=224308 GN=abnA PE=1 SV=3
P95470 2.64e-14 39 416 33 330
Extracellular exo-alpha-(1->5)-L-arabinofuranosidase ArbA OS=Cellvibrio japonicus (strain Ueda107) OX=498211 GN=arbA PE=1 SV=1
B3EYM8 5.23e-09 43 340 26 248
Intracellular endo-alpha-(1->5)-L-arabinanase OS=Geobacillus stearothermophilus OX=1422 GN=abnB PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.060577 0.564075 0.372242 0.001603 0.000745 0.000735

TMHMM  Annotations      download full data without filtering help

start end
9 28
900 922